GBRR2_HUMAN
ID GBRR2_HUMAN Reviewed; 465 AA.
AC P28476; A2BDE4; Q9H153;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 5.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit rho-2;
DE AltName: Full=GABA(A) receptor subunit rho-2;
DE AltName: Full=GABA(C) receptor;
DE Flags: Precursor;
GN Name=GABRR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=1315307; DOI=10.1016/0888-7543(92)90312-g;
RA Cutting G.R., Curristin S., Zoghbi H., O'Hara B., Seldin M.F., Uhl G.R.;
RT "Identification of a putative gamma-aminobutyric acid (GABA) receptor
RT subunit rho2 cDNA and colocalization of the genes encoding rho2 (GABRR2)
RT and rho1 (GABRR1) to human chromosome 6q14-q21 and mouse chromosome 4.";
RL Genomics 12:801-806(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate
CC brain, mediates neuronal inhibition by binding to the
CC GABA/benzodiazepine receptor and opening an integral chloride channel.
CC Rho-2 GABA receptor could play a role in retinal neurotransmission.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho. Interacts with SQSTM1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P28476-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28476-2; Sequence=VSP_044373;
CC -!- MISCELLANEOUS: [Isoform 2]: Isoform 2 could be translated from an
CC upstream initiator ATG located in frame within the first coding exon.
CC The probability of a signal peptide within this isoform is very low.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRR2 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; M86868; AAA52510.1; -; mRNA.
DR EMBL; AL121833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130352; AAI30353.1; -; mRNA.
DR EMBL; BC130354; AAI30355.1; -; mRNA.
DR CCDS; CCDS5020.3; -. [P28476-1]
DR PIR; A38079; A38079.
DR RefSeq; NP_002034.3; NM_002043.4. [P28476-1]
DR AlphaFoldDB; P28476; -.
DR SMR; P28476; -.
DR STRING; 9606.ENSP00000386029; -.
DR BindingDB; P28476; -.
DR ChEMBL; CHEMBL2375; -.
DR DrugBank; DB01567; Fludiazepam.
DR DrugCentral; P28476; -.
DR GlyGen; P28476; 2 sites.
DR iPTMnet; P28476; -.
DR PhosphoSitePlus; P28476; -.
DR BioMuta; GABRR2; -.
DR DMDM; 410516956; -.
DR EPD; P28476; -.
DR PaxDb; P28476; -.
DR PRIDE; P28476; -.
DR Antibodypedia; 18718; 123 antibodies from 23 providers.
DR DNASU; 2570; -.
DR Ensembl; ENST00000402938.4; ENSP00000386029.4; ENSG00000111886.11. [P28476-1]
DR GeneID; 2570; -.
DR KEGG; hsa:2570; -.
DR MANE-Select; ENST00000402938.4; ENSP00000386029.4; NM_002043.5; NP_002034.3.
DR UCSC; uc003pnb.4; human. [P28476-1]
DR CTD; 2570; -.
DR DisGeNET; 2570; -.
DR GeneCards; GABRR2; -.
DR HGNC; HGNC:4091; GABRR2.
DR HPA; ENSG00000111886; Tissue enriched (retina).
DR MIM; 137162; gene.
DR neXtProt; NX_P28476; -.
DR OpenTargets; ENSG00000111886; -.
DR PharmGKB; PA28506; -.
DR VEuPathDB; HostDB:ENSG00000111886; -.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000156864; -.
DR HOGENOM; CLU_010920_0_1_1; -.
DR InParanoid; P28476; -.
DR OMA; HIYKKNH; -.
DR OrthoDB; 640805at2759; -.
DR TreeFam; TF315453; -.
DR PathwayCommons; P28476; -.
DR Reactome; R-HSA-977443; GABA receptor activation.
DR SignaLink; P28476; -.
DR BioGRID-ORCS; 2570; 8 hits in 1072 CRISPR screens.
DR ChiTaRS; GABRR2; human.
DR GeneWiki; GABRR2; -.
DR GenomeRNAi; 2570; -.
DR Pharos; P28476; Tchem.
DR PRO; PR:P28476; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P28476; protein.
DR Bgee; ENSG00000111886; Expressed in vena cava and 131 other tissues.
DR Genevisible; P28476; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:1902711; C:GABA-A receptor complex; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004890; F:GABA-A receptor activity; TAS:ProtInc.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR008059; GABAAa_rho2_rcpt.
DR InterPro; IPR008057; GABAAa_rho_rcpt.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR01670; GABAARRHO.
DR PRINTS; PR01672; GABAARRHO2.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 2: Evidence at transcript level;
KW Alternative initiation; Cell membrane; Chloride; Chloride channel;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..465
FT /note="Gamma-aminobutyric acid receptor subunit rho-2"
FT /id="PRO_0000000488"
FT TOPO_DOM 21..260
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 178..192
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MVKPGGICSATGYWKAAFCLTDVHKM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044373"
FT CONFLICT 209
FT /note="Y -> H (in Ref. 1; AAA52510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 54151 MW; 209700077636A395 CRC64;
MPYFTRLILF LFCLMVLVES RKPKRKRWTG QVEMPKPSHL YKKNLDVTKI RKGKPQQLLR
VDEHDFSMRP AFGGPAIPVG VDVQVESLDS ISEVDMDFTM TLYLRHYWKD ERLAFSSASN
KSMTFDGRLV KKIWVPDVFF VHSKRSFTHD TTTDNIMLRV FPDGHVLYSM RITVTAMCNM
DFSHFPLDSQ TCSLELESYA YTDEDLMLYW KNGDESLKTD EKISLSQFLI QKFHTTSRLA
FYSSTGWYNR LYINFTLRRH IFFFLLQTYF PATLMVMLSW VSFWIDRRAV PARVSLGITT
VLTMTTIITG VNASMPRVSY VKAVDIYLWV SFVFVFLSVL EYAAVNYLTT VQERKERKLR
EKFPCMCGML HSKTMMLDGS YSESEANSLA GYPRSHILTE EERQDKIVVH LGLSGEANAA
RKKGLLKGQT GFRIFQNTHA IDKYSRLIFP ASYIFFNLIY WSVFS
